Mercaptoalkanoyl and acylmercaptoalkanoyl .alpha.-amino acids are disclosed as anti-hypertensive agents due to their angiotensin converting enzyme inhibition activity by Ondetti et al. in U.S. Pat. No. 4,053,651.
Cushman et al. (Biochemistry, Vol. 16, No. 25, 1977, p. 5484-5491) disclose various carboxyalkanoyl and mercaptoalkanoyl amino acids including ##STR1## as angiotensin converting enzyme inhibitors.
Greenberg et al. in U.S. Pat. No. 4,401,677 disclose that various mercaptoalkanoyl .alpha.-amino acids are useful analgesic agents due to their enkephalinase inhibition activity.
Sundeen et al. in U.S. Pat. No. 4,235,885 and 4,382,081 disclose that certain mercaptoalkanoyl and acylmercaptoalkanoyl amino acids inhibit mammalian collagenase and are thus useful in treating rheumatoid arthritis.
Delaney et al. in European Patent Application 136,883 disclose that mercaptoalkanoyl and acylmercaptoalkanoyl amino acids are useful analgesic agents due to their enkephalinase inhibition activity.
Roques et al. (Nature, Vol. 288, Nov. 1980, p. 286-288) disclose that thiorphan, [(D,L)-3- mercapto-2-benzylpropanol]glycine, is an inhibitor of enkephalinase in vitro in nanomolar concentrations and in vivo after either intracerebroventricular or systemic administration.
Roques et al. [Proc. Natl. Acad. Sci (U.S.A.) Vol. 80, 1983, p. 3178-3182]disclose thiorphan and its retro-inverso isomer, and their activity as inhibitors of enkephalinase.
Roques et al. in U.S. Pat. No. 4,513,009 disclose various .alpha.-amino acid derivatives including mercaptoalkanoyl and acylmercaptoalkanoyl derivatives as possessing enkephalinase inhibition activity.
Delaney et al. in European Patent Application 161,769 disclose mercapto and acylmercapto enkephalinase inhibitors of the formula ##STR2##
Weller et al. in U.S. Pat. No. 4,560,506 disclose that mercaptocycloalkanoyl, acylmercaptocycloalkanoyl, mercaptoarylcarbonyl, and acylmercaptoarylcarbonyl dipeptides possess angiotensin converting enzyme inhibition activity and depending upon the terminal amino acid may also possess enkephalinase inhibition activity.
Ondetti et al. Australian Patent 537,592 disclose mercaptoalkanoyl and acylmercaptoalkanoyl dipeptides possessing angiotensin converting enzyme inhibition activity.
Gordon et al. in U.S. Pat. No. 4,499,079 disclose that carboxycycloalkylcarbonyl dipeptides possess angiotensin converting enzyme inhibition activity and depending upon the terminal amino acid may also possess enkephalinase inhibition activity.
Berger in U.S. Pat. No. 4,610,816 disclose that carboxyalkyl dipeptides possess enkephalinase inhibition activity.
Mumford et al. (Biochemical and Biophysical Research Comm., Vol. 109, No. 4, 1982, p. 1303-1309) disclose that various substituted N-carboxymethyl dipeptides including those having a terminal .beta.-alanine group possess enkephalinase inhibition activity.
Ksander in PCT Application WO 86/00066 disclose that various carboxyacyl amino acids possess enkephalinase inhibition activity.
Thorsett et al. in U.S. Pat. No. 4,316,896 disclose that phosphoramides including the dipeptides of the formula ##STR3## possess angiotensin converting enzyme inhibition activity.
Karanewsky et al. in U.S. Pat. No. 4,432,972 disclose that phosphonamidates including the dipeptides of the formula ##STR4## possess angiotensin converting enzyme and enkephalinase inhibition activity.
Karanewsky et al. in U.S. Pat. No. 4,616,005 disclose phosphonate substituted amino acids of the formula ##STR5## possess angiotensin converting enzyme inhibition activity.
Gaeta in European Patent Application 117,429 disclose phosphorus containing enkephalinase inhibitors of the formula ##STR6## wherein W is R.sup.1 or OR.sup.1, X is -(CH.sub.2).sub.p -CHR.sup.3 or -CHR.sup.3 -(CH.sub.2).sub.p -, Y is ##STR7## and Z includes -(CHR.sup.4).sub.r.
Wilkinson et al. in U.S. Pat. No. 4,423,242 disclose enkephalinase inhibitors of the formula ##STR8## wherein Y is ##STR9## and R.sup.a and R.sup.b are independently selected from hydrogen, alkali metal salt ion, or alkyl.
Ryono et al. in U.S. Pat. No. 4,452,791 disclose angiotensin converting enzyme inhibitors including those of the formula ##STR10## wherein n is zero or one, R.sub.1 is alkyl, aryl, aralkyl, etc., and R.sub.3 is -(CH.sub.2).sub.m -NH.sub.2, ##STR11## wherein m is zero or an integer from 1 to 5.
Roques et al. in U.S. Pat. No. 4,618,708 disclose enkephalinase inhibitors including those of the formulas ##STR12##
Ondetti et al. in U.S. Pat. No. 4,105,789 disclose hydroxamic acid amino acids of the formula ##STR13##
Wilkinson et al. in U.S. Pat. No. 4,504,492 disclose enkephalinase inhibiting hydroxamic acids of the formula ##STR14## wherein Y is ##STR15##
Ura et al. (Kidney International, Vol. 29, No. 1) disclose that phosphoramidon caused changes in kidney function including decreased urinary kininase activity, increased excretion of kinins, increased urine volume, and increased sodium excretion. These actions are attributed to the ability of phosphoramidon to block the degradation of intrarenally generated kinins through the inhibition of neutral endopeptidase.
Elliott et al. (Journal of Medicinal Chemistry, Vol. 28, p 1208-1216, 1985) disclose the enkephalinase and angiotensin converting enzyme inhibition activity of various phosphonamidate dipeptides.
Stephenson et al. (Biochem. J., Vol. 243, p. 183-187) disclose that the hydrolysis of .alpha.-human atrial natriuretic peptide by pig kidney microvillar membranes in vitro was suppressed by phosphoramidon.